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P08148

- GP63_LEIMA

UniProt

P08148 - GP63_LEIMA

Protein

Leishmanolysin

Gene

gp63

Organism
Leishmania major
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Has an integral role during the infection of macrophages in the mammalian host.

    Catalytic activityi

    Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi264 – 2641Zinc; catalytic
    Active sitei265 – 2651
    Metal bindingi268 – 2681Zinc; catalytic
    Metal bindingi334 – 3341Zinc; catalytic

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM08.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leishmanolysin (EC:3.4.24.36)
    Alternative name(s):
    Cell surface protease
    Major surface glycoprotein
    Major surface protease
    Promastigote surface endopeptidase
    Protein gp63
    Gene namesi
    Name:gp63
    OrganismiLeishmania major
    Taxonomic identifieri5664 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi254 – 2541Y → D: No significant effect on protein expression levels or catalytic activity. 1 Publication
    Mutagenesisi264 – 2641H → F or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
    Mutagenesisi265 – 2651E → D: No significant effect on protein expression levels but almost abolishes catalytic activity. 1 Publication
    Mutagenesisi268 – 2681H → N or Y: No detectable overexpression of mutant protein and hence little catalytic activity. 1 Publication
    Mutagenesisi300 – 3001N → Q: Increases electrophoretic mobility of the protein. 1 Publication
    Mutagenesisi407 – 4071N → Q: Increases electrophoretic mobility of the protein. 1 Publication
    Mutagenesisi534 – 5341N → Q: Increases electrophoretic mobility of the protein. 1 Publication
    Mutagenesisi577 – 5771N → L: Causes extracellular release of the protein. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Sequence AnalysisAdd
    BLAST
    Propeptidei40 – 10061Activation peptide1 PublicationPRO_0000028667Add
    BLAST
    Chaini101 – 577477LeishmanolysinPRO_0000028668Add
    BLAST
    Propeptidei578 – 60225Removed in mature formPRO_0000028669Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi125 ↔ 1421 Publication
    Disulfide bondi191 ↔ 2301 Publication
    Glycosylationi300 – 3001N-linked (GlcNAc...)2 Publications
    Disulfide bondi314 ↔ 3861 Publication
    Disulfide bondi393 ↔ 4551 Publication
    Disulfide bondi406 ↔ 4251 Publication
    Glycosylationi407 – 4071N-linked (GlcNAc...)2 Publications
    Disulfide bondi415 ↔ 4891 Publication
    Disulfide bondi466 ↔ 5101 Publication
    Disulfide bondi515 ↔ 5651 Publication
    Glycosylationi534 – 5341N-linked (GlcNAc...)1 Publication
    Disulfide bondi535 ↔ 5581 Publication
    Lipidationi577 – 5771GPI-anchor amidated asparagine1 Publication

    Post-translational modificationi

    The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

    PTM databases

    UniCarbKBiP08148.

    Miscellaneous databases

    PMAP-CutDBP08148.

    Structurei

    Secondary structure

    1
    602
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi111 – 1144
    Helixi116 – 1194
    Beta strandi131 – 1333
    Beta strandi135 – 1373
    Beta strandi139 – 1413
    Helixi144 – 1463
    Helixi150 – 1589
    Helixi160 – 16910
    Beta strandi172 – 1743
    Beta strandi177 – 1815
    Helixi191 – 1933
    Helixi198 – 2025
    Beta strandi205 – 2073
    Beta strandi209 – 2157
    Beta strandi226 – 2327
    Beta strandi238 – 2447
    Helixi247 – 2493
    Helixi256 – 26914
    Helixi274 – 2796
    Beta strandi283 – 2875
    Helixi289 – 2913
    Beta strandi296 – 2994
    Helixi302 – 31211
    Beta strandi320 – 3223
    Turni328 – 3325
    Beta strandi333 – 3353
    Turni337 – 3393
    Beta strandi346 – 3483
    Helixi356 – 3649
    Helixi372 – 3743
    Turni380 – 3834
    Helixi386 – 3905
    Beta strandi393 – 3953
    Beta strandi398 – 4003
    Turni402 – 4043
    Beta strandi420 – 4256
    Helixi435 – 4373
    Beta strandi440 – 4423
    Turni450 – 4545
    Beta strandi458 – 4658
    Helixi470 – 4723
    Turni475 – 4773
    Helixi478 – 4803
    Beta strandi487 – 4948
    Beta strandi506 – 51611
    Turni517 – 5204
    Beta strandi521 – 5255
    Beta strandi540 – 5423
    Helixi543 – 5453
    Beta strandi548 – 5503
    Beta strandi555 – 5573
    Helixi561 – 5655
    Helixi569 – 5724

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LMLX-ray1.86A100-577[»]
    ProteinModelPortaliP08148.
    SMRiP08148. Positions 100-574.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08148.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M8 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR001577. Peptidase_M8.
    [Graphical view]
    PANTHERiPTHR10942. PTHR10942. 1 hit.
    PfamiPF01457. Peptidase_M8. 1 hit.
    [Graphical view]
    PRINTSiPR00782. LSHMANOLYSIN.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08148-1 [UniParc]FASTAAdd to Basket

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    MSVDSSSTHR RRCVAARLVR LAAAGAAVTV AVGTAAAWAH AGALQHRCVH    50
    DAMQARVRQS VADHHKAPGA VSAVGLPYVT LDAAHTAAAA DPRPGSARSV 100
    VRDVNWGALR IAVSTEDLTD PAYHCARVGQ HVKDHAGAIV TCTAEDILTN 150
    EKRDILVKHL IPQAVQLHTE RLKVQQVQGK WKVTDMVGDI CGDFKVPQAH 200
    ITEGFSNTDF VMYVASVPSE EGVLAWATTC QTFSDGHPAV GVINIPAANI 250
    ASRYDQLVTR VVTHEMAHAL GFSGPFFEDA RIVANVPNVR GKNFDVPVIN 300
    SSTAVAKARE QYGCDTLEYL EVEDQGGAGS AGSHIKMRNA QDELMAPAAA 350
    AGYYTALTMA IFQDLGFYQA DFSKAEVMPW GQNAGCAFLT NKCMEQSVTQ 400
    WPAMFCNESE DAIRCPTSRL SLGACGVTRH PGLPPYWQYF TDPSLAGVSA 450
    FMDYCPVVVP YSDGSCTQRA SEAHASLLPF NVFSDAARCI DGAFRPKATD 500
    GIVKSYAGLC ANVQCDTATR TYSVQVHGSN DYTNCTPGLR VELSTVSNAF 550
    EGGGYITCPP YVEVCQGNVQ AAKDGGNTAA GRRGPRAAAT ALLVAALLAV 600
    AL 602
    Length:602
    Mass (Da):63,953
    Last modified:April 1, 1990 - v2
    Checksum:i982EF3245D87C43E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00647 Genomic DNA. Translation: CAA68673.1.
    PIRiPL0221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00647 Genomic DNA. Translation: CAA68673.1 .
    PIRi PL0221.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LML X-ray 1.86 A 100-577 [» ]
    ProteinModelPortali P08148.
    SMRi P08148. Positions 100-574.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M08.001.

    PTM databases

    UniCarbKBi P08148.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P08148.
    PMAP-CutDB P08148.

    Family and domain databases

    InterProi IPR001577. Peptidase_M8.
    [Graphical view ]
    PANTHERi PTHR10942. PTHR10942. 1 hit.
    Pfami PF01457. Peptidase_M8. 1 hit.
    [Graphical view ]
    PRINTSi PR00782. LSHMANOLYSIN.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the major surface antigen of leishmania."
      Button L.L., McMaster W.R.
      J. Exp. Med. 167:724-729(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 101-123.
    2. Button L.L., McMaster W.R.
      J. Exp. Med. 171:589-589(1990)
      Cited for: SEQUENCE REVISION.
    3. "Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease."
      Schneider P., Ferguson M.A.J., McConville M.J., Mehlert A., Homans S.W., Bordier C.
      J. Biol. Chem. 265:16955-16964(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT ASN-577.
    4. "Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit."
      McGwire B.S., Chang K.-P.
      J. Biol. Chem. 271:7903-7909(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-254; HIS-264; GLU-265; HIS-268; ASN-300; ASN-407; ASN-534 AND ASN-577.
    5. "A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces."
      Funk V.A., Thomas-Oates J.E., Kielland S.L., Bates P.A., Olafson R.W.
      Mol. Biochem. Parasitol. 84:33-48(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-300 AND ASN-407.
    6. "Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major."
      Schlagenhauf E., Etges R., Metcalf P.
      Proteins 22:58-66(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-300; ASN-407 AND ASN-534.
    7. "The crystal structure of the Leishmania major surface proteinase leishmanolysin."
      Schlagenhauf E., Etges R., Metcalf P.
      Structure 6:1035-1046(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).

    Entry informationi

    Entry nameiGP63_LEIMA
    AccessioniPrimary (citable) accession number: P08148
    Secondary accession number(s): P15906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3